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Identification of amino acids in highly pathogenic avian influenza H5N1 virus hemagglutinin that determine avian influenza species specificity.

Abstract：

:To test the role of neutralizing antibodies (nAbs) and receptor adaptation in interspecies transmission of influenza virus, two H5N1 strains, isolated from human and avian hosts, with four amino acid differences in hemagglutinin (HA) and seven HA mutations were studied. We found that a mutation at amino acid position 90 in the H5N1 HA, outside the receptor-binding domain (RBD), could simultaneously induce changes in the RBD conformation to escape from nAb binding and alter the receptor preference through long-range regulation. This mutation was deemed a "key event" for interspecies transmission. It is likely a result of positive selection caused by antibodies, allowing the original invasion by new species-specific variants. A mutation at amino acid position 160 in the RBD only induced a change in receptor preference. This mutation was deemed a "maintaining adaptation", which ensured that influenza virus variants would be able to infect new organisms of a different species successfully. The mutation is the result of adaptation caused by the receptor. Our results suggest that continuing occurrence of these two types of mutations made the variants persist in the new host species.

journal_name

Arch Virol

journal_title

Archives of virology

authors

Li Z,Liu Z,Ma C,Zhang L,Su Y,Gao GF,Li Z,Cui L,He W

doi

10.1007/s00705-011-1056-2

subject

Has Abstract

pub_date

2011-10-01 00:00:00

pages

1803-12

issue

10

eissn

0304-8608

issn

1432-8798

journal_volume

156

pub_type

杂志文章

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